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Seed protein content and composition of near-isogenic and induced mutant pea lines

Published online by Cambridge University Press:  19 September 2008

M. D. Perez ,
S. J. Chambers ,
J. R. Bacon ,
N. Lambert ,
C. L. Hedley  and
T. L. Wang
M. D. Perez
Affiliation:
Veterinary Faculty, University of Zaragoza, Spain
S. J. Chambers
Affiliation:
AFRC Institute of Food Research, Department of Food Molecular Biochemistry, Norwich Laboratory, Norwich Research Park, Colney, Norwich, UK,
J. R. Bacon
Affiliation:
AFRC Institute of Food Research, Department of Food Molecular Biochemistry, Norwich Laboratory, Norwich Research Park, Colney, Norwich, UK,
N. Lambert
Affiliation:
AFRC Institute of Food Research, Department of Food Molecular Biochemistry, Norwich Laboratory, Norwich Research Park, Colney, Norwich, UK,
C. L. Hedley
Affiliation:
John Innes Institute, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK
T. L. Wang*
Affiliation:
John Innes Institute, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK
*
* Correspondence
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Abstract

Total protein content and amounts of albumin, legumin and vicilin have been determined for pea seeds from lines near-isogenic except for genes at the rugosus loci, r and rb (RR/RbRb; rr/RbRb; RR/rbrb; rr/rbrb). Seeds with the wildtype, round-seeded phenotype (RR/RbRb) had less protein on a total seed dry-weight basis than any of the wrinkled-seeded lines and this protein had a lower proportion of albumin. The lines which had recessive alleles at both r and rb loci had the highest proportion of protein and the highest proportion of albumin. The roundseeded peas possessed nearly two-fold more legumin than the double recessive line, with proportions for the two single recessive lines falling in between these extremes. Vicilin levels were similarfor all four near-isogenic lines. SDS-PAGE analysis of the isolated albumin, legumin and vicilin fractions revealed no significant differences between the four lines. Differential scanning calorimetry of protein extracts showed that all the wrinkled-seeded near-isolines possessed legumin fractions with diminished thermal stability relative to that from the roundseeded, wild-type line.

Chemically-induced mutants were also analysed for protein content and composition. These mutants have previously been shown to display great variation in starch and lipid levels. Total protein varied from 20.3% to 37.9%; however, relative proportions of albumin, legumin and vicilin were similar in all mutant lines. SDS-PAGE analysis identified two mutant pea lines which possessed a legumin A-chain of 65 000 Mr as well as the typical 45 000 Mr form. Differential scanning calorimetry of protein extracts indicated that the legumin in all mutants had lower enthalpies of denaturation than the legumin in the round-seeded parent.

The mutant pea lines possess exceptional variation with respect to starch, lipid and protein which raises opportunities for their use in the food and animal feedstuff industries.

Keywords

Genetic variationmutantsnear-isogenicpeaPisum sativumprotein
Type
Research Papers
Information
Seed Science Research , Volume 3 , Issue 3 , September 1993 , pp. 187 - 194
Copyright
Copyright © Cambridge University Press 1993

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References

Arthur, A.E., Adams, H., Strouts, K., Jones, D.A., Wang, T.L. and Hedley, C.L. (1991) An analysis of seed development in Pisum sativum XV: The influence of seed size on protein content. Seed Science Research 1, 203–208.CrossRefGoogle Scholar
Bilidt, H. (1990) Functional ingredients from the yellow field pea, pp 219–222in Turner, A. (Ed.) Food Technology International. Sterling Publishing Group, London.Google Scholar
Casey, R., Sharman, J.E., Wright, D.J., Bacon, J.R. and Guldager, P. (1982) Quantitative variability in Pisum seed globulins: its assessment and significance. Qualitas Plantarium Plant Foods for Human Nutrition 31, 333–346.CrossRefGoogle Scholar
Casey, R., Domoney, C. and Ellis, N. (1986) Legume storage proteins and their genes. Plant Molecular Cell Biology 3, 1–95.Google Scholar
Chambers, S.J., Bacon, J.R. and Lambert, N. (1992) The quantitative analysis of seed proteins from peas using high performance liquid chromotography.Phytochemical Analysis 3, 49–54.CrossRefGoogle Scholar
Croy, R.R.D., Gatehouse, J.A., Tyler, M. and Boulter, D. (1980) The purification and characterisation of a third storage protein from the seeds of pea. Biochemical Journal 191, 509–516.CrossRefGoogle ScholarPubMed
Croy, R.R.D., Hoque, M.S., Gatehouse, J.A. and Boulter, D. (1984) The major albumin proteins from pea. Biochemical Journal 218, 795–803.CrossRefGoogle ScholarPubMed
Dagorn-Scaviner, C., Gueguen, J. and Lefebvre, J. (1986) A comparison of interfacial behaviours of pea legumin and vicilin at air-water interfaces. Die Nahrung 30, 337–347.CrossRefGoogle Scholar
Gatehouse, J.A., Croy, R.R.D. and Boulter, D. (1984) The synthesis and structure for pea storage proteins. CRC Critical Reviews in Plant Science 1, 287–314.CrossRefGoogle Scholar
Gueguen, J. (1983) Legume seed protein extraction, processing and end product characteristics. Qualitas Plantarium Plant Foods for Human Nutrition 32, 267–303.CrossRefGoogle Scholar
Gueguen, J. and Barbot, J. (1988) Quantitative and qualitative variability of pea protein composition. Journal of the Science of Food and Agriculture 42, 209–224.CrossRefGoogle Scholar
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.CrossRefGoogle ScholarPubMed
Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) Protein measurement with the Folin-Phenol reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle ScholarPubMed
Monti, L.M. and Grillo, S. (1983) Legume seed improvement for protein content and quality. Qualitas Plantarium Plant Foods for Human Nutrition 32, 253–266.CrossRefGoogle Scholar
Mossé, J. and Baudet, J. (1983) Crude protein and amino acid composition of seeds: variability and correlations. Qualitas Plantarium Plant Foods for Human Nutrition 32, 225–245.CrossRefGoogle Scholar
Nakamura, T., Utsumi, S. and Mori, T. (1985) Formation of pseudoglycinins from intermediary subunits of glycinin and their gel properties and network structure. Agricultural Biological Chemistry 49, 2733–2740.Google Scholar
Nakamura, T., Utsumi, S. and Mori, T. (1986) Mechanism of heat-induced gelation and gel properties of soybean 7S globulin. Agricultural Biological Chemistry 50, 1287–1293.Google Scholar
Nielson, S.S., Deshpande, S.S., Hermodson, M.A. and Scott, M.P. (1988) Comparative digestibility of legume storage proteins. Journal of Agricultural and Food Chemistry 36, 896–902.CrossRefGoogle Scholar
Schroeder, H.E. (1982) Quantitative studies on the cotyledonary proteins in the genus Pisum. Journal of the Science of Food and Agriculture 33, 623–633.CrossRefGoogle ScholarPubMed
Schroeder, H.E. (1984) Major albumins of Pisum cotyledons.Journal of the Science of Food and Agriculture 35, 191–198.CrossRefGoogle ScholarPubMed
Smith, A.M. (1988) Major differences in isoforms of starch-branching enzyme between developing embryos of round and wrinkled-seeded peas. Planta 175, 270–279.CrossRefGoogle ScholarPubMed
Smith, A.M., Bettey, M. and Bedford, I.D. (1989) Evidence that rb locus alters the starch content of developing pea embryos through an effect on ADP glucose pyrophosphorylase. Plant Physiology 89, 1279–1284.CrossRefGoogle ScholarPubMed
Turner, S.R., Barratt, D.H.P. and Casey, R. (1990) The effect of different alleles at ther locus on the synthesis of seed storage proteins in Pisum sativum. Plant Molecular Biology 14, 793–803.CrossRefGoogle Scholar
Utsumi, S., Damodaran, S. and Kinsella, J.E. (1984) Heat induced interactions between soybean proteins: preferential association of 11S basic subunits and β subunits of 7S. Journal of Agricultural and Food Chemistry 32, 1406–1412.CrossRefGoogle Scholar
Wang, T.L., Hadavizideh, A., Harwood, A., Welham, T.J., Harwood, W.A., Faulks, R. and Hedley, C.L. (1990) An analysis of seed development in Pisum sativum. XIII. Chemical induction of storage product mutants. Plant Breeding 105, 311–320.CrossRefGoogle Scholar
Wang, T.L. and Hedley, C.L. (1991) Seed development in peas: knowing your three ‘r’s (or four, or five) Seed Science Research 1, 3–14.Google Scholar
Wright, D.J. (1987) The seed globulins. pp 81–157in Hudson, B.J.F. (Ed.) Developments in Food Proteins. London, Elsevier Applied Science.Google Scholar
Wright, D.J. and Boulter, D. (1980) Differential scanning calorimetric study of meals and constituents of some food grain legumes. Journal of the Science of Food and Agriculture 31, 1231–1241.CrossRefGoogle Scholar